ID F9YR81_CAPCC Unreviewed; 860 AA.
AC F9YR81;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Ccan_03170 {ECO:0000313|EMBL:AEK22439.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22439.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK22439.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP002113; AEK22439.1; -; Genomic_DNA.
DR RefSeq; WP_013996434.1; NC_015846.1.
DR AlphaFoldDB; F9YR81; -.
DR STRING; 860228.Ccan_03170; -.
DR KEGG; ccm:Ccan_03170; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000008895; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:AEK22439.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 97298 MW; F05A87AB343AE232 CRC64;
MNFNNYTIKS QEVVQRAQQI AQSYGHQELQ NEHFFKAIEE VDQNVLPFLL KKLNINREQL
SKVLETALQS FPKVSGGQMS LSREANTMLN EAVNIAKKMN DEYVSIEHLI LAIFKSNSKI
GQALKDQGVK EKDLEKAIQE LRKGERVTSA SAEETYNSLN KYAKNLNQMA DSGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVQGDVPENL KDKSIYSLDM
GALIAGAKYK GEFEERLKSV VKEVTSSDGN IILFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKEKYETHHK
VRIKDEAIIA AVELSERYIT NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE NDEQKLKMLY ADVANLKEER NAIFAKWQSE KNVIDEVQTT KEAIENYKLE
AEKAEREGDY AKVAELRYGK IKEAQDNLVL LQEKLDQAQG NSLIKEEVTS ENIAEVVAKW
TGIPVTKMLQ GEREKLLKLE SELHKRVVGQ EEAIEAISDA IRRSKAGLQD PKKPIGSFLF
LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHAV SRLVGAPPGY VGYDEGGQLT
EAVRRRPYSV ILLDEIEKAH PDTFNILLQV LDEGRLTDNK GRTADFKNTI IIMTSNIGSH
LIQESFEKYT NDLEKATEVA KDDVLQLLKQ TVRPEFINRI DDIVMFTPLS RENIRSIVRL
QLRSIIKMVA RENILLDATD QAIDYLAEKG FDPQFGARPV KRTLQKEVLN RLSKEILSGN
IHKDKTILLD TFDNQLVFRN
//